ID A0A2N6NGW0_BEABA Unreviewed; 652 AA.
AC A0A2N6NGW0;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=AMP deaminase {ECO:0000256|ARBA:ARBA00012775};
DE EC=3.5.4.6 {ECO:0000256|ARBA:ARBA00012775};
GN Name=ada1 {ECO:0000313|EMBL:PMB66518.1};
GN ORFNames=BM221_007510 {ECO:0000313|EMBL:PMB66518.1};
OS Beauveria bassiana (White muscardine disease fungus) (Tritirachium
OS shiotae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=176275 {ECO:0000313|EMBL:PMB66518.1, ECO:0000313|Proteomes:UP000235728};
RN [1] {ECO:0000313|EMBL:PMB66518.1, ECO:0000313|Proteomes:UP000235728}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEF-007 {ECO:0000313|EMBL:PMB66518.1,
RC ECO:0000313|Proteomes:UP000235728};
RX PubMed=27470140; DOI=10.1007/s00253-016-7734-y;
RA Kim S., Lee S.J., Nai Y.S., Yu J.S., Lee M.R., Yang Y.T., Kim J.S.;
RT "Characterization of T-DNA insertion mutants with decreased virulence in
RT the entomopathogenic fungus Beauveria bassiana JEF-007.";
RL Appl. Microbiol. Biotechnol. 100:8889-8900(2016).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via salvage pathway; IMP
CC from AMP: step 1/1. {ECO:0000256|ARBA:ARBA00004955}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Adenosine and AMP deaminases family. {ECO:0000256|ARBA:ARBA00006676,
CC ECO:0000256|PIRNR:PIRNR001251}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PMB66518.1}.
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DR EMBL; MRVG01000008; PMB66518.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N6NGW0; -.
DR OMA; RKERGMC; -.
DR UniPathway; UPA00591; UER00663.
DR Proteomes; UP000235728; Unassembled WGS sequence.
DR GO; GO:0003876; F:AMP deaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0032264; P:IMP salvage; IEA:UniProtKB-UniPathway.
DR CDD; cd01319; AMPD; 1.
DR Gene3D; 4.10.800.20; -; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR InterPro; IPR006650; A/AMP_deam_AS.
DR InterPro; IPR006329; AMPD.
DR InterPro; IPR032466; Metal_Hydrolase.
DR NCBIfam; TIGR01429; AMP_deaminase; 1.
DR PANTHER; PTHR11359; AMP DEAMINASE; 1.
DR PANTHER; PTHR11359:SF0; AMP DEAMINASE; 1.
DR Pfam; PF19326; AMP_deaminase; 1.
DR PIRSF; PIRSF001251; AMP_deaminase_met; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR PROSITE; PS00485; A_DEAMINASE; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000235728}.
FT REGION 552..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 580..611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 628..652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 555..571
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..606
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 629..652
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 652 AA; 74853 MW; C5BAB75BADACE59B CRC64;
MDNLMPLPGD DDCTFELDSN GVYQILDNES ATEPAIRIPT IREFYMDLES ILKVSSDGPS
KSFAFRRLQY LEGKFNLYAL LNEYQETADS KKVPHRDFYN VRKVDTHVHH SACMNQKHLL
RFIKSKMKKY PNEVVLYRDG KHLTLAEVFA SINLTAYDLS IDTLDMHAHT DSFHRFDKFN
LKYNPIGESR LRTIFLKTDN FIHGRYLAEI TKEVIEDLES SKYQMVEWRI SIYGKSIDEW
DKLAAWVVDN KLFSHNVRWL IQIPRLYDVY KGSGLMDSFE QVIKNLFQPL FEVTKDPASH
PKLHVFLQRV IGFDSVDDES KVERRLFRKF PVPREWDGAQ NPPYSYWIYY TFANMASLNF
WRKKRGFNTF TLRPHCGEAG DSEHLAVAAL CCHSISHGLL LRKVPLLQYI FYLEQIGMAM
SPLSNNALFL SYERNPFHQY FKRGLNVSLS TDDPLQFAFT KEPLIEEYAV AAQICKLSSV
DMCELAKNSV KQSGYERAIK QQWLGPDFEK PGKEGNKMVK TNVPDRRAEF RYITLVQERD
VLRRFSAYEA NNDSGMLKKP NNQASAHSCS QVLSSLSNNT GPLGKLGTEH GVPFGEDARH
SDSSTDLRLT GSDPRLFPGI LAREHHIGSL KSLSQSQEDS ANSNDKAGMS AS
//